WO 2013/064736 Al 10 May 2013 (10.05.2013) P O P CT

Total Page:16

File Type:pdf, Size:1020Kb

WO 2013/064736 Al 10 May 2013 (10.05.2013) P O P CT (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization I International Bureau (10) International Publication Number (43) International Publication Date WO 2013/064736 Al 10 May 2013 (10.05.2013) P O P CT (51) International Patent Classification: BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, C12N 9/10 (2006.01) DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, (21) International Application Number: KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, PCT/FI2012/05 1048 ME, MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, (22) International Filing Date: NO, NZ, OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, 3 1 October 2012 (3 1.10.2012) RW, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, (25) Filing Language: English ZM, ZW. (26) Publication Language: English (84) Designated States (unless otherwise indicated, for every (30) Priority Data: kind of regional protection available): ARIPO (BW, GH, 201 16074 1 November 201 1 (01. 11.201 1) FI GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, SZ, TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, (71) Applicant: VALIO LTD [FI/FI]; Meijeritie 6, FI-00370 TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, DK, Helsinki (FI). EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, SM, (72) Inventors: RAJAKARI, Kirsi; c/o Valio Ltd, Meijeritie 6, TR), OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, FI-00370 Helsinki (FI). HOTAKAINEN, Kai; c/o Valio ML, MR, NE, SN, TD, TG). Ltd, Meijeritie 6, FI-00370 Helsinki (FI). MYLLARINEN, Paivi; c/o Valio Ltd, Meijeritie 6, FI- Declarations under Rule 4.17 : 00370 Helsinki (FI). — as to applicant's entitlement to apply for and be granted a (74) Agent: KOLSTER OY AB; ISO Roobertinkatu 23, P.O. patent (Rule 4.1 7(H)) Box 148, FI-00121 Helsinki (FI). Published: (81) Designated States (unless otherwise indicated, for every — with international search report (Art. 21(3)) kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, © (54) Title: A LIQUID ENZYME FORMULATION AND A PROCESS FOR ITS PREPARATION (57) Abstract: The present invention relates to a liquid enzyme formulation, particularly to a liquid and stable formulation compris - ing a crosslinking enzyme and/or an enzyme modifying milk proteins. Particularly the present invention relates a liquid and stable S transglutaminase formulation. In addition, the present invention relates to a method for preparing a liquid enzyme formulation. A LIQUID ENZYME FORMULATION AND A PROCESS FOR ITS PREPARATION FIELD OF THE INVENTION [0001] The present invention relates to a liquid enzyme formulation, particularly to a liquid and stable formulation comprising a crosslinking enzyme and/or an enzyme modifying milk proteins. Particularly the present invention relates a liquid and stable transglutaminase formulation. In addition, the pre sent invention relates to a method for preparing a liquid enzyme formulation. BACKGROUND OF THE INVENTION [0002] Enzyme formulations comprising a crosslinking enzyme and/or an enzyme modifying milk proteins, such as laccase, tyrosinase, perox idase, sulfhydryl oxidase or glucose oxidase are commercially available both in powder and liquid formulations. However, transglutaminase and protein glu- taminase products are currently in the market only in powder form. The use of a powdered enzyme product is not totally accepted due to the dust formation in all production plants. The health hazards resulting from the dusting have in curred concerns among the workers, especially. [0003] A transglutaminase derived from Streptoverticillium moba- raense strain and a process for its preparation has been disclosed in the Euro pean patent No. 0 379 606 B 1 . Further, a method for the production of a transglutaminase using a gene isolated from Streptomyces lydicus strain is disclosed in the European Patent No. 0 777 726 B 1 . [0004] One of the problems associated with formulating an enzyme, such as a transglutaminase, in liquid form, is the lack of stability of the formula tion. Further, one of the disadvantages associated with the present liquid e n zyme formulations is that they contain at least one preservative. BRIEF DESCRIPTION OF THE INVENTION [0005] An object of the present invention is thus to provide a liquid enzyme formulation comprising transglutaminase and/or another milk protein crosslinking and/or modifying enzyme such as laccase, tyrosinase, peroxidase, sulfhydryl oxidase, glucose oxidase or protein glutaminase, which is stable and can be stored for a time period required from a commercial formulation in a room temperature or in temperatures of a refrigerator and/or a freezer. [0006] Another object of the present invention is to provide a liquid formulation comprising a transglutaminase, which is stable and can be stored for a time period required from a commercial formulation in a room tempera ture or in temperatures of a refrigerator and/or a freezer. [0007] A further object of the present invention is to provide a meth od for the preparation of a stable, liquid enzyme formulation comprising trans glutaminase and/or another milk protein crosslinking and/or modifying enzyme. [0008] An even further object of the present invention is to provide a method for the preparation of a stable, liquid formulation comprising a transglu taminase. [0009] The objects of the invention are achieved by the formulations and methods set forth in the independent claims. Preferred embodiments of the invention are described in the dependent claims. [0010] Other objects, details and advantages of the present inven tion will become apparent from the following detailed description and examples. DETAILED DESCRIPTION OF THE INVENTION [001 1] Milk protein crosslinking and/or modifying enzymes such as transglutaminase, laccase, tyrosinase, peroxidase, sulfhydryl oxidase and pro tein glutaminase catalyze milk protein modifications. There seems to be syner gism within the action of these enzymes and further with the action of glucose oxidase. Without being bound by any theory glucose oxidase and/or peroxi dase seem to catalyze reactions wherein oxygen is released through hydrogen peroxide formation. The oxygen can then catalyze (oxidate) crosslinking of ty rosinase. [0012] Milk protein crosslinking and/or modifying enzymes such as transglutaminase, laccase, tyrosinase, peroxidase, sulfhydryl oxidase and pro tein glutaminase optionally together with glucose oxidase are used in the man ufacture of processed fish, meat and egg products, pastes and pates, fruits, berries and vegetables, soy products, cereal products, bread and bakery prod ucts. [0013] Following milk protein crosslinking and/or modifying enzymes are all relevant in food prosessing in dairy or other food categories. [0014] Transglutaminases are a family of enzymes (EC 2.3.2.1 3) that catalyze the generation of covalent linkages between the glutamine and lysine amino acid residues present in the protein molecules. When linkages are formed, ammonia is released. [0015] Laccases (EC 1. 1 0.3.2) derived from fungi and bacteria, such as, fungus Trametes hirsute, catalyze the crosslinking between carbohy drates and proteins (oxidation of aromatic compounds and cysteine) with a p plications in food processing for reduction of allergenicity, for example. [0016] Tyrosinases (EC 1.14.1 8.1 ) are enzymes which catalyzes the oxidation of phenols such as tyrosine, with applications in food processing for reduction of allergenicity, for example. [0017] Peroxidases (EC 1. 1 1. 1 .7) are a family of enzymes that cata lyze the oxidation of aromatic compounds with applications in food processing for reduction of allergenicity, for example. [0018] Sulfhydryl oxidase (EC 1.8.3.3) catalyzes the formation of d i sulfide bonds, oxidation of glutathione. [0019] Protein glutaminase catalyzes the deamidation of protein bound glutamine, and glutamine is converted to glutamic acid. [0020] Glucose oxidase catalyzes the formation of protein crosslinks and oxidative gelation of pentosans. [0021] Milk protein crosslinking and/or modifying enzymes such as transglutaminase, laccase, tyrosinase, peroxidase, sulfhydryl oxidase and pro tein glutaminase are used in dairy industry to stabilize the structure of milk- based products. In addition to dairy industry, these enzymes are used in the manufacture of processed fish, meat and egg products, pastes and pates, fruits, berries and vegetables, soy products, cereal products, bread and bakery products. Accordingly, a liquid enzyme formulation is suited for the manufac ture of dairy, processed fish, meat, egg, pastes and pates, fruits, berries and vegetables, soy, cereal, bread and bakery products, for example. The use of a liquid enzyme preparation would be more practical and advantageous than the use of powder formulation, especially in the industrial scale manufacturing. [0022] Transglutaminases are most active in the pH range from 5.2 to 8 . When a liquidized transglutaminase is stored at pH 5.2 or at pH 8, the enzyme loses its activity quickly. After storing a transglutaminase at pH 5.2 for 7 days at room temperature or in the temperature of a refrigerator, only half of the activity is left. [0023] The invention is based on the finding that when a transglu taminase, tyrosinase or protein glutaminase is stored in a suspension of a polyol, such as glycerol or sorbitol, and water in the pH range from 4.4 to 5.1 , its activity is remained moderately during storage at room temperature and excellently during storage in the temperatures of a refrigerator and/or a freezer. In addition, the invention is based on the finding that when a transglutaminase together with a protein glutaminase is stored in a suspen sion of glycerol and water at pH 4.6, the activity of the enzymes remained moderately during storage at room temperature and excellently during sto r age in the temperatures of a refrigerator and/or a freezer.
Recommended publications
  • Rational Design of Resveratrol O-Methyltransferase for the Production of Pinostilbene
    International Journal of Molecular Sciences Article Rational Design of Resveratrol O-methyltransferase for the Production of Pinostilbene Daniela P. Herrera 1 , Andrea M. Chánique 1,2 , Ascensión Martínez-Márquez 3, Roque Bru-Martínez 3 , Robert Kourist 2 , Loreto P. Parra 4,* and Andreas Schüller 4,5,* 1 Department of Chemical and Bioprocesses Engineering, School of Engineering, Pontificia Universidad Católica de Chile, Vicuña Mackenna 4860, Santiago 7820244, Chile; [email protected] (D.P.H.); [email protected] (A.M.C.) 2 Institute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria; [email protected] 3 Department of Agrochemistry and Biochemistry, Faculty of Science and Multidisciplinary Institute for Environmental Studies “Ramon Margalef”, University of Alicante, 03690 Alicante, Spain; [email protected] (A.M.-M.); [email protected] (R.B.-M.) 4 Institute for Biological and Medical Engineering, Schools of Engineering, Medicine and Biological Sciences, Pontificia Universidad Católica de Chile, Vicuña Mackenna 4860, Santiago 7820244, Chile 5 Department of Molecular Genetics and Microbiology, School of Biological Sciences, Pontificia Universidad Católica de Chile, Av. Libertador Bernardo O’Higgins 340, Santiago 8320000, Chile * Correspondence: [email protected] (L.P.P.); [email protected] (A.S.) Abstract: Pinostilbene is a monomethyl ether analog of the well-known nutraceutical resveratrol. Both compounds have health-promoting properties, but the latter undergoes rapid metabolization and has low bioavailability. O-methylation improves the stability and bioavailability of resveratrol. In plants, these reactions are performed by O-methyltransferases (OMTs). Few efficient OMTs that Citation: Herrera, D.P.; Chánique, monomethylate resveratrol to yield pinostilbene have been described so far.
    [Show full text]
  • Table 2. Significant
    Table 2. Significant (Q < 0.05 and |d | > 0.5) transcripts from the meta-analysis Gene Chr Mb Gene Name Affy ProbeSet cDNA_IDs d HAP/LAP d HAP/LAP d d IS Average d Ztest P values Q-value Symbol ID (study #5) 1 2 STS B2m 2 122 beta-2 microglobulin 1452428_a_at AI848245 1.75334941 4 3.2 4 3.2316485 1.07398E-09 5.69E-08 Man2b1 8 84.4 mannosidase 2, alpha B1 1416340_a_at H4049B01 3.75722111 3.87309653 2.1 1.6 2.84852656 5.32443E-07 1.58E-05 1110032A03Rik 9 50.9 RIKEN cDNA 1110032A03 gene 1417211_a_at H4035E05 4 1.66015788 4 1.7 2.82772795 2.94266E-05 0.000527 NA 9 48.5 --- 1456111_at 3.43701477 1.85785922 4 2 2.8237185 9.97969E-08 3.48E-06 Scn4b 9 45.3 Sodium channel, type IV, beta 1434008_at AI844796 3.79536664 1.63774235 3.3 2.3 2.75319499 1.48057E-08 6.21E-07 polypeptide Gadd45gip1 8 84.1 RIKEN cDNA 2310040G17 gene 1417619_at 4 3.38875643 1.4 2 2.69163229 8.84279E-06 0.0001904 BC056474 15 12.1 Mus musculus cDNA clone 1424117_at H3030A06 3.95752801 2.42838452 1.9 2.2 2.62132809 1.3344E-08 5.66E-07 MGC:67360 IMAGE:6823629, complete cds NA 4 153 guanine nucleotide binding protein, 1454696_at -3.46081884 -4 -1.3 -1.6 -2.6026947 8.58458E-05 0.0012617 beta 1 Gnb1 4 153 guanine nucleotide binding protein, 1417432_a_at H3094D02 -3.13334396 -4 -1.6 -1.7 -2.5946297 1.04542E-05 0.0002202 beta 1 Gadd45gip1 8 84.1 RAD23a homolog (S.
    [Show full text]
  • Biosynthetic Investigation of Phomopsins Reveals a Widespread Pathway for Ribosomal Natural Products in Ascomycetes
    Biosynthetic investigation of phomopsins reveals a widespread pathway for ribosomal natural products in Ascomycetes Wei Dinga, Wan-Qiu Liua, Youli Jiaa, Yongzhen Lia, Wilfred A. van der Donkb,c,1, and Qi Zhanga,b,1 aDepartment of Chemistry, Fudan University, Shanghai 200433, China; bDepartment of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; and cHoward Hughes Medical Institute, University of Illinois at Urbana–Champaign, Urbana, IL 61801 Edited by Jerrold Meinwald, Cornell University, Ithaca, NY, and approved February 23, 2016 (received for review November 24, 2015) Production of ribosomally synthesized and posttranslationally mod- dehydroaspartic acid, 3,4-dehydroproline, and 3,4-dehydrovaline ified peptides (RiPPs) has rarely been reported in fungi, even (Fig. 1A). though organisms of this kingdom have a long history as a prolific Early isotopic labeling studies showed that Ile, Pro, and Phe were source of natural products. Here we report an investigation of the all incorporated into the phomopsin scaffold (24). Because a Phe phomopsins, antimitotic mycotoxins. We show that phomopsin is a hydroxylase that can convert Phe to Tyr has not been found in fungal RiPP and demonstrate the widespread presence of a path- Ascomycetes, the labeling study seems incongruent with a ribosomal way for the biosynthesis of a family of fungal cyclic RiPPs, which we route to phomopsins, in which Tyr, not Phe, would need to be in- term dikaritins. We characterize PhomM as an S-adenosylmethionine– corporated into the phomopsin structure via a tRNA-dependent dependent α-N-methyltransferase that converts phomopsin A to pathway. Here we report our investigation of the biosynthetic path- an N,N-dimethylated congener (phomopsin E), and show that the way of phomopsins, which explains the paradoxical observations in methyltransferases involved in dikaritin biosynthesis have evolved the early labeling studies and unequivocally demonstrates that pho- differently and likely have broad substrate specificities.
    [Show full text]
  • National Coverage Determination Procedure Code: 82977 Gamma Glutamyl Transferase CMS Policy Number: 190.32 Back to NCD List
    National Coverage Determination Procedure Code: 82977 Gamma Glutamyl Transferase CMS Policy Number: 190.32 Back to NCD List Description: Gamma glutamyl transferase (GGT) is an intracellular enzyme that appears in blood following leakage from cells. Renal tubules, liver, and pancreas contain high amounts, although the measurement of GGT in serum is almost always used for assessment of Hepatobiliary function. Unlike other enzymes which are found in heart, skeletal muscle, and intestinal mucosa as well as liver, the appearance of an elevated level of GGT in serum is almost always the result of liver disease or injury. It is specifically useful to differentiate elevated alkaline phosphatase levels when the source of the alkaline phosphatase increase (bone, liver, or placenta) is unclear. The combination of high alkaline phosphatase and a normal GGT does not, however, rule out liver disease completely. As well as being a very specific marker of Hepatobiliary function, GGT is also a very sensitive marker for hepatocellular damage. Abnormal concentrations typically appear before elevations of other liver enzymes or biliuria are evident. Obstruction of the biliary tract, viral infection (e.g., hepatitis, mononucleosis), metastatic cancer, exposure to hepatotoxins (e.g., organic solvents, drugs, alcohol), and use of drugs that induce microsomal enzymes in the liver (e.g., cimetidine, barbiturates, phenytoin, and carbamazepine) all can cause a moderate to marked increase in GGT serum concentration. In addition, some drugs can cause or exacerbate liver dysfunction (e.g., atorvastatin, troglitazone, and others as noted in FDA Contraindications and Warnings.) GGT is useful for diagnosis of liver disease or injury, exclusion of hepatobiliary involvement related to other diseases, and patient management during the resolution of existing disease or following injury.
    [Show full text]
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
    [Show full text]
  • Relating Metatranscriptomic Profiles to the Micropollutant
    1 Relating Metatranscriptomic Profiles to the 2 Micropollutant Biotransformation Potential of 3 Complex Microbial Communities 4 5 Supporting Information 6 7 Stefan Achermann,1,2 Cresten B. Mansfeldt,1 Marcel Müller,1,3 David R. Johnson,1 Kathrin 8 Fenner*,1,2,4 9 1Eawag, Swiss Federal Institute of Aquatic Science and Technology, 8600 Dübendorf, 10 Switzerland. 2Institute of Biogeochemistry and Pollutant Dynamics, ETH Zürich, 8092 11 Zürich, Switzerland. 3Institute of Atmospheric and Climate Science, ETH Zürich, 8092 12 Zürich, Switzerland. 4Department of Chemistry, University of Zürich, 8057 Zürich, 13 Switzerland. 14 *Corresponding author (email: [email protected] ) 15 S.A and C.B.M contributed equally to this work. 16 17 18 19 20 21 This supporting information (SI) is organized in 4 sections (S1-S4) with a total of 10 pages and 22 comprises 7 figures (Figure S1-S7) and 4 tables (Table S1-S4). 23 24 25 S1 26 S1 Data normalization 27 28 29 30 Figure S1. Relative fractions of gene transcripts originating from eukaryotes and bacteria. 31 32 33 Table S1. Relative standard deviation (RSD) for commonly used reference genes across all 34 samples (n=12). EC number mean fraction bacteria (%) RSD (%) RSD bacteria (%) RSD eukaryotes (%) 2.7.7.6 (RNAP) 80 16 6 nda 5.99.1.2 (DNA topoisomerase) 90 11 9 nda 5.99.1.3 (DNA gyrase) 92 16 10 nda 1.2.1.12 (GAPDH) 37 39 6 32 35 and indicates not determined. 36 37 38 39 S2 40 S2 Nitrile hydration 41 42 43 44 Figure S2: Pearson correlation coefficients r for rate constants of bromoxynil and acetamiprid with 45 gene transcripts of ECs describing nucleophilic reactions of water with nitriles.
    [Show full text]
  • The Neurochemical Consequences of Aromatic L-Amino Acid Decarboxylase Deficiency
    The neurochemical consequences of aromatic L-amino acid decarboxylase deficiency Submitted By: George Francis Gray Allen Department of Molecular Neuroscience UCL Institute of Neurology Queen Square, London Submitted November 2010 Funded by the AADC Research Trust, UK Thesis submitted for the degree of Doctor of Philosophy, University College London (UCL) 1 I, George Allen confirm that the work presented in this thesis is my own. Where information has been derived from other sources, I confirm that this has been indicated in the thesis. Signed………………………………………………….Date…………………………… 2 Abstract Aromatic L-amino acid decarboxylase (AADC) catalyses the conversion of 5- hydroxytryptophan (5-HTP) and L-3,4-dihydroxyphenylalanine (L-dopa) to the neurotransmitters serotonin and dopamine respectively. The inherited disorder AADC deficiency leads to a severe deficit of serotonin and dopamine as well as an accumulation of 5-HTP and L-dopa. This thesis investigated the potential role of 5- HTP/L-dopa accumulation in the pathogenesis of AADC deficiency. Treatment of human neuroblastoma cells with L-dopa or dopamine was found to increase intracellular levels of the antioxidant reduced glutathione (GSH). However inhibiting AADC prevented the GSH increase induced by L-dopa. Furthermore dopamine but not L-dopa, increased GSH release from human astrocytoma cells, which do not express AADC activity. GSH release is the first stage of GSH trafficking from astrocytes to neurons. This data indicates dopamine may play a role in controlling brain GSH levels and consequently antioxidant status. The inability of L-dopa to influence GSH concentrations in the absence of AADC or with AADC inhibited indicates GSH trafficking/metabolism may be compromised in AADC deficiency.
    [Show full text]
  • (P -Value<0.05, Fold Change≥1.4), 4 Vs. 0 Gy Irradiation
    Table S1: Significant differentially expressed genes (P -Value<0.05, Fold Change≥1.4), 4 vs. 0 Gy irradiation Genbank Fold Change P -Value Gene Symbol Description Accession Q9F8M7_CARHY (Q9F8M7) DTDP-glucose 4,6-dehydratase (Fragment), partial (9%) 6.70 0.017399678 THC2699065 [THC2719287] 5.53 0.003379195 BC013657 BC013657 Homo sapiens cDNA clone IMAGE:4152983, partial cds. [BC013657] 5.10 0.024641735 THC2750781 Ciliary dynein heavy chain 5 (Axonemal beta dynein heavy chain 5) (HL1). 4.07 0.04353262 DNAH5 [Source:Uniprot/SWISSPROT;Acc:Q8TE73] [ENST00000382416] 3.81 0.002855909 NM_145263 SPATA18 Homo sapiens spermatogenesis associated 18 homolog (rat) (SPATA18), mRNA [NM_145263] AA418814 zw01a02.s1 Soares_NhHMPu_S1 Homo sapiens cDNA clone IMAGE:767978 3', 3.69 0.03203913 AA418814 AA418814 mRNA sequence [AA418814] AL356953 leucine-rich repeat-containing G protein-coupled receptor 6 {Homo sapiens} (exp=0; 3.63 0.0277936 THC2705989 wgp=1; cg=0), partial (4%) [THC2752981] AA484677 ne64a07.s1 NCI_CGAP_Alv1 Homo sapiens cDNA clone IMAGE:909012, mRNA 3.63 0.027098073 AA484677 AA484677 sequence [AA484677] oe06h09.s1 NCI_CGAP_Ov2 Homo sapiens cDNA clone IMAGE:1385153, mRNA sequence 3.48 0.04468495 AA837799 AA837799 [AA837799] Homo sapiens hypothetical protein LOC340109, mRNA (cDNA clone IMAGE:5578073), partial 3.27 0.031178378 BC039509 LOC643401 cds. [BC039509] Homo sapiens Fas (TNF receptor superfamily, member 6) (FAS), transcript variant 1, mRNA 3.24 0.022156298 NM_000043 FAS [NM_000043] 3.20 0.021043295 A_32_P125056 BF803942 CM2-CI0135-021100-477-g08 CI0135 Homo sapiens cDNA, mRNA sequence 3.04 0.043389246 BF803942 BF803942 [BF803942] 3.03 0.002430239 NM_015920 RPS27L Homo sapiens ribosomal protein S27-like (RPS27L), mRNA [NM_015920] Homo sapiens tumor necrosis factor receptor superfamily, member 10c, decoy without an 2.98 0.021202829 NM_003841 TNFRSF10C intracellular domain (TNFRSF10C), mRNA [NM_003841] 2.97 0.03243901 AB002384 C6orf32 Homo sapiens mRNA for KIAA0386 gene, partial cds.
    [Show full text]
  • Discovery of Oxidative Enzymes for Food Engineering. Tyrosinase and Sulfhydryl Oxi- Dase
    Dissertation VTT PUBLICATIONS 763 1,0 0,5 Activity 0,0 2 4 6 8 10 pH Greta Faccio Discovery of oxidative enzymes for food engineering Tyrosinase and sulfhydryl oxidase VTT PUBLICATIONS 763 Discovery of oxidative enzymes for food engineering Tyrosinase and sulfhydryl oxidase Greta Faccio Faculty of Biological and Environmental Sciences Department of Biosciences – Division of Genetics ACADEMIC DISSERTATION University of Helsinki Helsinki, Finland To be presented for public examination with the permission of the Faculty of Biological and Environmental Sciences of the University of Helsinki in Auditorium XII at the University of Helsinki, Main Building, Fabianinkatu 33, on the 31st of May 2011 at 12 o’clock noon. ISBN 978-951-38-7736-1 (soft back ed.) ISSN 1235-0621 (soft back ed.) ISBN 978-951-38-7737-8 (URL: http://www.vtt.fi/publications/index.jsp) ISSN 1455-0849 (URL: http://www.vtt.fi/publications/index.jsp) Copyright © VTT 2011 JULKAISIJA – UTGIVARE – PUBLISHER VTT, Vuorimiehentie 5, PL 1000, 02044 VTT puh. vaihde 020 722 111, faksi 020 722 4374 VTT, Bergsmansvägen 5, PB 1000, 02044 VTT tel. växel 020 722 111, fax 020 722 4374 VTT Technical Research Centre of Finland, Vuorimiehentie 5, P.O. Box 1000, FI-02044 VTT, Finland phone internat. +358 20 722 111, fax + 358 20 722 4374 Edita Prima Oy, Helsinki 2011 2 Greta Faccio. Discovery of oxidative enzymes for food engineering. Tyrosinase and sulfhydryl oxi- dase. Espoo 2011. VTT Publications 763. 101 p. + app. 67 p. Keywords genome mining, heterologous expression, Trichoderma reesei, Aspergillus oryzae, sulfhydryl oxidase, tyrosinase, catechol oxidase, wheat dough, ascorbic acid Abstract Enzymes offer many advantages in industrial processes, such as high specificity, mild treatment conditions and low energy requirements.
    [Show full text]
  • Metabolic Engineering of Escherichia Coli for Natural Product Biosynthesis
    Trends in Biotechnology Special Issue: Metabolic Engineering Review Metabolic Engineering of Escherichia coli for Natural Product Biosynthesis Dongsoo Yang,1,4 Seon Young Park,1,4 Yae Seul Park,1 Hyunmin Eun,1 and Sang Yup Lee1,2,3,∗ Natural products are widely employed in our daily lives as food additives, Highlights pharmaceuticals, nutraceuticals, and cosmetic ingredients, among others. E. coli has emerged as a prominent host However, their supply has often been limited because of low-yield extraction for natural product biosynthesis. from natural resources such as plants. To overcome this problem, metabolically Escherichia coli Improved enzymes with higher activity, engineered has emerged as a cell factory for natural product altered substrate specificity, and product biosynthesis because of many advantages including the availability of well- selectivity can be obtained by structure- established tools and strategies for metabolic engineering and high cell density based or computer simulation-based culture, in addition to its high growth rate. We review state-of-the-art metabolic protein engineering. E. coli engineering strategies for enhanced production of natural products in , Balancing the expression levels of genes together with representative examples. Future challenges and prospects of or pathway modules is effective in natural product biosynthesis by engineered E. coli are also discussed. increasing the metabolic flux towards target compounds. E. coli as a Cell Factory for Natural Product Biosynthesis System-wide analysis of metabolic Natural products have been widely used in food and medicine in human history. Many of these networks, omics analysis, adaptive natural products have been developed as pharmaceuticals or employed as structural backbones laboratory evolution, and biosensor- based screening can further increase for the development of new drugs [1], and also as food and cosmetic ingredients.
    [Show full text]
  • Enrichment, Isolation and Characterization of Phenazine-1-Carboxylic Acid (PCA)-Degrading Bacteria Under Aerobic and Anaerobic Conditions
    Enrichment, isolation and characterization of phenazine-1-carboxylic acid (PCA)-degrading bacteria under aerobic and anaerobic conditions Miaomiao Zhang A thesis in fulfilment of the requirements for the degree of Doctor of Philosophy School of Civil and Environmental Engineering Faculty of Engineering September, 2018 THE UNIVERSITY OF NEW SOUTH WALES Thesis/Dissertation Sheet Surname or Family name: ZHANG First name: Miaomiao Other name/s: Abbreviation for degree as given in the University calendar: PhD School: Civil and Environmental Engineering Faculty: Engineering Title: Enrichment, isolation and characterization of phenazine-1- carboxylic acid (PCA)-degrading bacteria under aerobic and anaerobic conditions Abstract Phenazines are a large class of nitrogen-containing aromatic heterocyclic compounds produced and secreted by bacteria from phylogenetically diverse taxa under aerobic and anaerobic conditions. Phenazine-1-carboxylic acid (PCA) is regarded as a ‘core’ phenazine because it is transformed to other phenazine derivatives. Due to their important roles in ecological fitness, biocontrol of plant pathogens, infection in cystic fibrosis and potential in anticancer treatments, understanding the fate of phenazine compounds is prudent. Only seven bacterial species are known to degrade phenazines and all of them are aerobic. Hence, the aim of this study is to enrich, isolate and characterize additional bacteria with the ability to degrade phenazines aerobically and anaerobically. In this study, the isolation of a PCA-degrading Rhodanobacter sp. PCA2 belonging to Grammaproteobacteria is reported. Characterization studies revealed that strain PCA2 is also capable of transforming other phenazines including phenazine, pyocyanin and 1-hydroxyphenazine. The sequencing, annotation and analysis of the genome of strain PCA2 revealed that genes (ubiD and the homolog of the MFORT_16269 gene) involved in PCA degradation were plasmid borne.
    [Show full text]
  • Amino Acid Degradation
    BI/CH 422/622 OUTLINE: OUTLINE: Protein Degradation (Catabolism) Digestion Amino-Acid Degradation Inside of cells Protein turnover Dealing with the carbon Ubiquitin Fates of the 29 Activation-E1 Seven Families Conjugation-E2 nitrogen atoms in 20 1. ADENQ Ligation-E3 AA: Proteosome 2. RPH 9 ammonia oxidase Amino-Acid Degradation 18 transamination Ammonia 2 urea one-carbon metabolism free transamination-mechanism to know THF Urea Cycle – dealing with the nitrogen SAM 5 Steps Carbamoyl-phosphate synthetase 3. GSC Ornithine transcarbamylase PLP uses Arginino-succinate synthetase Arginino-succinase 4. MT – one carbon metabolism Arginase 5. FY – oxidase vs oxygenase Energetics Urea Bi-cycle 6. KW – Urea Cycle – dealing with the nitrogen 7. BCAA – VIL Feeding the Urea Cycle Glucose-Alanine Cycle Convergence with Fatty acid-odd chain Free Ammonia Overview Glutamine Glutamate dehydrogenase Overall energetics Amino Acid A. Concepts 1. ConvergentDegradation 2. ketogenic/glucogenic 3. Reactions seen before The SEVEN (7) Families B. Transaminase (A,D,E) / Deaminase (Q,N) Family C. Related to biosynthesis (R,P,H; C,G,S; M,T) 1.Glu Family a. Introduce oxidases/oxygenases b. Introduce one-carbon metabolism (1C) 2.Pyruvate Family a. PLP reactions 3. a-Ketobutyric Family (M,T) a. 1-C metabolism D. Dedicated 1. Aromatic Family (F,Y) a. oxidases/oxygenases 2. a-Ketoadipic Family (K,W) 3. Branched-chain Family (V,I,L) E. Convergence with Fatty Acids: propionyl-CoA 29 N 1 Amino Acid Degradation • Intermediates of the central metabolic pathway • Some amino acids result in more than one intermediate. • Ketogenic amino acids can be converted to ketone bodies.
    [Show full text]